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UniProtKB - Q9ALJ4 (AGAA_GEOSE)

Entry version 64 (07 Apr 2021)
Sequence version 1 (01 Jun 2001)
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Protein

Alpha-galactosidase AgaA

Gene

agaA

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Hydrolyzes the short-chain alpha-galactosaccharides raffinose and stachyose.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.3 Publications EC:3.2.1.22

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Not inhibited by D-galactose or sucrose (Ref. 1). Inhibited by pharmaceutical drug 1-deoxygalactonojirimycin (PubMed:23012371).2 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 105 s(-1) for p-nitrophenyl-alpha-galactopyranoside (at 25 degrees Celsius and pH 6.5). kcat is 180 s(-1) for raffinose (at 25 degrees Celsius and pH 6.5).1 Publication
  1. KM=0.21 mM for p-nitrophenyl-alpha-galactopyranoside (at 25 degrees Celsius and pH 6.5)1 Publication
  2. KM=3.8 mM for raffinose (at 25 degrees Celsius and pH 6.5)1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 65 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei53SubstrateCombined sources1 Publication1
    Binding sitei199SubstrateCombined sources1 Publication1
    Binding sitei443SubstrateCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei478Nucleophile1 Publication1
    Binding sitei526SubstrateCombined sources1 Publication1
    Active sitei548Proton donor1 Publication1
    Binding sitei548SubstrateCombined sources1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionGlycosidase, Hydrolase
    Biological processCarbohydrate metabolism

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...    CAZyi    		GH36, Glycoside Hydrolase Family 36

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Alpha-galactosidase AgaA1 PublicationImported (EC:3.2.1.223 Publications)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:agaA1 PublicationImported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)Imported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1422 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Has properties that make it suitable for elimination of D-raffinose from low green syrup in sugar manufacturing process from beets in order to improve the yield of sucrose.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi336W → A: Very strongly reduced hydrolytic efficiency against raffinose, but displays medium level of transglycosylation activity compared to none with wild-type enzyme. 1 Publication1
    Mutagenesisi336W → F or S: Strongly reduced hydrolytic efficiency against raffinose, but displays high level of transglycosylation activity compared to none with wild-type enzyme. 1 Publication1
    Mutagenesisi336W → N: Very strongly reduced hydrolytic efficiency against raffinose, but displays low level of transglycosylation activity compared to none with wild-type enzyme. 1 Publication1
    Mutagenesisi478D → A: Loss of activity. 1 Publication1
    Mutagenesisi548D → N: Loss of activity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004395851 – 729Alpha-galactosidase AgaAAdd BLAST729

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer.

    By similarity

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1729
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		Q9ALJ4

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Protein Data Bank in Europe - Knowledge Base

    More...    PDBe-KBi    		Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni366 – 367Substrate bindingCombined sources1 Publication2
    Regioni476 – 480Substrate bindingCombined sources1 Publication5

    <p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the glycosyl hydrolase 36 family.Curated

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd14791, GH36, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		2.60.40.1180, 1 hit
    2.70.98.60, 1 hit
    3.20.20.70, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR013785, Aldolase_TIM
    IPR038417, Alpga-gal_N_sf
    IPR000111, Glyco_hydro_27/36_CS
    IPR002252, Glyco_hydro_36
    IPR031705, Glyco_hydro_36_C
    IPR031704, Glyco_hydro_36_N
    IPR013780, Glyco_hydro_b
    IPR017853, Glycoside_hydrolase_SF

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF16874, Glyco_hydro_36C, 1 hit
    PF16875, Glyco_hydro_36N, 1 hit

    PIRSF; a whole-protein classification database

    More...    PIRSFi    		PIRSF005536, Agal, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00743, GLHYDRLASE36

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF51445, SSF51445, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00512, ALPHA_GALACTOSIDASE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    Q9ALJ4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSVAYNPQTK QFHLRAGKAS YVMQLFRSGY LAHVYWGKAV RDVRGARAFP 
            60         70         80         90        100
    RLDRAFSPNP DPSDRTFSLD TLLQEYPAYG NTDFRAPAYQ VQLENGSTVT 
           110        120        130        140        150
    DLRYKTHRIY KGKPRLNGLP ATYVEHEQEA ETLEIVLGDA LIGLEVTLQY 
           160        170        180        190        200
    TAYEKWNVIT RSARFENKGG ERLKLLRALS MSVDFPTADY DWIHLPGAWG 
           210        220        230        240        250
    RERWIERRPL VTGVQAAESR RGASSHQQNP FIALVAKNAD EHQGEVYGFS 
           260        270        280        290        300
    FVYSGNFLAQ IEVDQFGTAR VSMGINPFDF TWLLQPGESF QTPEVVMVYS 
           310        320        330        340        350
    DQGLNGMSQT YHELYRTRLA RGAFRDRERP ILINNWEATY FDFNEEKIVN 
           360        370        380        390        400
    IARTAAELGI ELVVLDDGWF GERDDDRRSL GDWIVNRRKL PNGLDGLAKQ 
           410        420        430        440        450
    VNELGLQFGL WVEPEMVSPN SELYRKHPDW CLHVPNRPRS EGRNQLVLDY 
           460        470        480        490        500
    SREDVCDYII ETISNVLASA PITYVKWDMN RHMTEIGSSA LPPERQRETA 
           510        520        530        540        550
    HRYMLGLYRV MDEITSRFPH ILFESCSGGG GRFDPGMLYY MPQTWTSDNT 
           560        570        580        590        600
    DAVSRLKIQY GTSLVYPISA MGAHVSAVPN HQVGRVASLK TRGHVAMSGN 
           610        620        630        640        650
    FGYELDITKL TETEKQMMKQ QVAFYKDVRR LVQFGTFYRL LSPFEGNEAA 
           660        670        680        690        700
    WMFVSADRSE ALVAYFRVLA EANAPLSYLR LKGLDSNQDY EIEGLGVYGG 
           710        720 
    DELMYAGVAL PYRSSDFISM MWRLKAVQQ
    Length:729
    Mass (Da):83,211
    Last modified:June 1, 2001 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6E59129E1C3502A2
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		AY013286 Genomic DNA Translation: AAG49420.1

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		AY013286 Genomic DNA Translation: AAG49420.1

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4FNPX-ray2.80A/B/C/D1-729[»]
    4FNRX-ray3.20A/B/C/D1-729[»]
    4FNSX-ray2.60A/B/C/D1-729[»]
    4FNTX-ray2.60A/B/C/D1-729[»]
    4FNUX-ray3.60A/B/C/D1-729[»]
    SMRiQ9ALJ4
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    CAZyiGH36, Glycoside Hydrolase Family 36

    Family and domain databases

    CDDicd14791, GH36, 1 hit
    Gene3Di2.60.40.1180, 1 hit
    2.70.98.60, 1 hit
    3.20.20.70, 1 hit
    InterProiView protein in InterPro
    IPR013785, Aldolase_TIM
    IPR038417, Alpga-gal_N_sf
    IPR000111, Glyco_hydro_27/36_CS
    IPR002252, Glyco_hydro_36
    IPR031705, Glyco_hydro_36_C
    IPR031704, Glyco_hydro_36_N
    IPR013780, Glyco_hydro_b
    IPR017853, Glycoside_hydrolase_SF
    PfamiView protein in Pfam
    PF16874, Glyco_hydro_36C, 1 hit
    PF16875, Glyco_hydro_36N, 1 hit
    PIRSFiPIRSF005536, Agal, 1 hit
    PRINTSiPR00743, GLHYDRLASE36
    SUPFAMiSSF51445, SSF51445, 1 hit
    PROSITEiView protein in PROSITE
    PS00512, ALPHA_GALACTOSIDASE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAGAA_GEOSE
    <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9ALJ4
    <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2017
    Last sequence update: June 1, 2001
    Last modified: April 7, 2021
    This is version 64 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    <p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
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